Issue 19, 2020

Structure of micelle bound cationic peptides by NMR spectroscopy using a lanthanide shift reagent

Abstract

[Tm(DPA)3]3− was used to generate multiple, paramagnetic nuclear Overhauser effect NMR spectra of cationic peptides when weakly bound to a lipopolysaccharide micelle. Increased spectral resolution combined with a marked increase in the number of distance restraints yielded high resolution structures of polymyxin and MSI-594 in the liposaccharide bound state.

Graphical abstract: Structure of micelle bound cationic peptides by NMR spectroscopy using a lanthanide shift reagent

Supplementary files

Article information

Article type
Communication
Submitted
26 Nov 2019
Accepted
17 Jan 2020
First published
24 Jan 2020

Chem. Commun., 2020,56, 2897-2900

Structure of micelle bound cationic peptides by NMR spectroscopy using a lanthanide shift reagent

J. D. Swarbrick, J. A. Karas, J. Li and T. Velkov, Chem. Commun., 2020, 56, 2897 DOI: 10.1039/C9CC09207B

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